User:Karsten Theis/turns
From Proteopedia
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| - | A '''beta turn''' is a secondary structure element consisting of four consecutive amino acids (or three peptide planes). The geometry of turns correspond to a change in the direction of the polypeptide backbone, with a short distance between the first and fourth alpha carbon. This allows them to connect alpha helices and beta strands at the surface of a globular protein. Of the six main chain hydrogen bonding partners of a turn, a maximum of two are engaged in hydrogen bonding, and turns are rarely found in the hydrophobic core. | + | A '''beta turn''' is a secondary structure element consisting of four consecutive amino acids (or three consecutive peptide planes). The geometry of turns correspond to a change in the direction of the polypeptide backbone, with a short distance between the first and fourth alpha carbon. This allows them to connect alpha helices and beta strands at the surface of a globular protein. Of the six main chain hydrogen bonding partners of a turn, a maximum of two are engaged in hydrogen bonding, and turns are rarely found in the hydrophobic core. |
<ref>doi:10.3390/ijms232012314</ref> | <ref>doi:10.3390/ijms232012314</ref> | ||
Revision as of 17:41, 8 February 2025
A beta turn is a secondary structure element consisting of four consecutive amino acids (or three consecutive peptide planes). The geometry of turns correspond to a change in the direction of the polypeptide backbone, with a short distance between the first and fourth alpha carbon. This allows them to connect alpha helices and beta strands at the surface of a globular protein. Of the six main chain hydrogen bonding partners of a turn, a maximum of two are engaged in hydrogen bonding, and turns are rarely found in the hydrophobic core.
Exploring turns
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References
- ↑ de Brevern AG. A Perspective on the (Rise and Fall of) Protein β-Turns. Int J Mol Sci. 2022 Oct 14;23(20):12314. PMID:36293166 doi:10.3390/ijms232012314
